Full text data of WDR1
WDR1
[Confidence: low (only semi-automatic identification from reviews)]
WD repeat-containing protein 1 (Actin-interacting protein 1; AIP1; NORI-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WD repeat-containing protein 1 (Actin-interacting protein 1; AIP1; NORI-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75083
ID WDR1_HUMAN Reviewed; 606 AA.
AC O75083; A8K6E9; A8MPU4; O75313; Q8N6E5; Q9UG05; Q9UG78; Q9UQE0;
read moreDT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=WD repeat-containing protein 1;
DE AltName: Full=Actin-interacting protein 1;
DE Short=AIP1;
DE AltName: Full=NORI-1;
GN Name=WDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10036186; DOI=10.1006/geno.1998.5672;
RA Adler H.J., Winnicki R.S., Gong T.-W.L., Lomax M.I.;
RT "A gene upregulated in the acoustically damaged chick basilar papilla
RT encodes a novel WD40 repeat protein.";
RL Genomics 56:59-69(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphoid tissue;
RA Abe Y., Nezu K., Ueda N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-185.
RC TISSUE=Colon, Eye, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-17 (ISOFORMS 1/2).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-606 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PROTEIN SEQUENCE OF 290-306 (ISOFORMS 1/2), AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-81; LYS-95; LYS-115
RP AND LYS-480, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=22721921; DOI=10.1016/j.ejcb.2012.05.005;
RA Cervero P., Himmel M., Kruger M., Linder S.;
RT "Proteomic analysis of podosome fractions from macrophages reveals
RT similarities to spreading initiation centres.";
RL Eur. J. Cell Biol. 91:908-922(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction
CC with ADF/cofilin family proteins (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cell projection, podosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75083-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75083-3; Sequence=VSP_012926;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family.
CC -!- SIMILARITY: Contains 11 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05045.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
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DR EMBL; AF020056; AAD05044.1; -; mRNA.
DR EMBL; AF020260; AAD05045.1; ALT_SEQ; mRNA.
DR EMBL; AB010427; BAA31855.2; -; mRNA.
DR EMBL; AK291614; BAF84303.1; -; mRNA.
DR EMBL; AC005674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000201; AAH00201.1; -; mRNA.
DR EMBL; BC002489; AAH02489.1; -; mRNA.
DR EMBL; BC030541; AAH30541.1; -; mRNA.
DR EMBL; AL050108; CAB43276.1; -; mRNA.
DR EMBL; AL110208; CAB53674.2; -; mRNA.
DR PIR; T13152; T13152.
DR RefSeq; NP_005103.2; NM_005112.4.
DR RefSeq; NP_059830.1; NM_017491.3.
DR UniGene; Hs.128548; -.
DR ProteinModelPortal; O75083; -.
DR SMR; O75083; 8-606.
DR IntAct; O75083; 7.
DR STRING; 9606.ENSP00000382881; -.
DR PhosphoSite; O75083; -.
DR OGP; O75083; -.
DR REPRODUCTION-2DPAGE; IPI00746165; -.
DR REPRODUCTION-2DPAGE; O75083; -.
DR UCD-2DPAGE; O75083; -.
DR PaxDb; O75083; -.
DR PRIDE; O75083; -.
DR Ensembl; ENST00000382451; ENSP00000371889; ENSG00000071127.
DR Ensembl; ENST00000382452; ENSP00000371890; ENSG00000071127.
DR Ensembl; ENST00000499869; ENSP00000427687; ENSG00000071127.
DR Ensembl; ENST00000502702; ENSP00000426725; ENSG00000071127.
DR GeneID; 9948; -.
DR KEGG; hsa:9948; -.
DR UCSC; uc021xlv.1; human.
DR CTD; 9948; -.
DR GeneCards; GC04M010075; -.
DR HGNC; HGNC:12754; WDR1.
DR HPA; CAB020804; -.
DR MIM; 604734; gene.
DR neXtProt; NX_O75083; -.
DR PharmGKB; PA37358; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG000780; -.
DR OMA; NYWDSET; -.
DR OrthoDB; EOG7TXKG1; -.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; O75083; -.
DR ChiTaRS; WDR1; human.
DR GeneWiki; WDR1; -.
DR GenomeRNAi; 9948; -.
DR NextBio; 37534; -.
DR PRO; PR:O75083; -.
DR ArrayExpress; O75083; -.
DR Bgee; O75083; -.
DR CleanEx; HS_WDR1; -.
DR Genevestigator; O75083; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 606 WD repeat-containing protein 1.
FT /FTId=PRO_0000051341.
FT REPEAT 56 95 WD 1.
FT REPEAT 100 143 WD 2.
FT REPEAT 144 184 WD 3.
FT REPEAT 187 226 WD 4.
FT REPEAT 232 271 WD 5.
FT REPEAT 318 359 WD 6.
FT REPEAT 363 401 WD 7.
FT REPEAT 443 482 WD 8.
FT REPEAT 487 526 WD 9.
FT REPEAT 530 569 WD 10.
FT REPEAT 574 605 WD 11.
FT MOD_RES 28 28 N6-acetyllysine.
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 95 95 N6-acetyllysine.
FT MOD_RES 115 115 N6-acetyllysine.
FT MOD_RES 238 238 Phosphotyrosine.
FT MOD_RES 480 480 N6-acetyllysine.
FT VAR_SEQ 47 186 Missing (in isoform 2).
FT /FTId=VSP_012926.
FT VARIANT 185 185 I -> V (in dbSNP:rs13441).
FT /FTId=VAR_013445.
SQ SEQUENCE 606 AA; 66194 MW; 8C08C31D5CD097F1 CRC64;
MPYEIKKVFA SLPQVERGVS KIIGGDPKGN NFLYTNGKCV ILRNIDNPAL ADIYTEHAHQ
VVVAKYAPSG FYIASGDVSG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGAV FLWDSGSSVG EITGHNKVIN SVDIKQSRPY RLATGSDDNC AAFFEGPPFK
FKFTIGDHSR FVNCVRFSPD GNRFATASAD GQIYIYDGKT GEKVCALGGS KAHDGGIYAI
SWSPDSTHLL SASGDKTSKI WDVSVNSVVS TFPMGSTVLD QQLGCLWQKD HLLSVSLSGY
INYLDRNNPS KPLHVIKGHS KSIQCLTVHK NGGKSYIYSG SHDGHINYWD SETGENDSFA
GKGHTNQVSR MTVDESGQLI SCSMDDTVRY TSLMLRDYSG QGVVKLDVQP KCVAVGPGGY
AVVVCIGQIV LLKDQRKCFS IDNPGYEPEV VAVHPGGDTV AIGGVDGNVR LYSILGTTLK
DEGKLLEAKG PVTDVAYSHD GAFLAVCDAS KVVTVFSVAD GYSENNVFYG HHAKIVCLAW
SPDNEHFASG GMDMMVYVWT LSDPETRVKI QDAHRLHHVS SLAWLDEHTL VTTSHDASVK
EWTITY
//
ID WDR1_HUMAN Reviewed; 606 AA.
AC O75083; A8K6E9; A8MPU4; O75313; Q8N6E5; Q9UG05; Q9UG78; Q9UQE0;
read moreDT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 139.
DE RecName: Full=WD repeat-containing protein 1;
DE AltName: Full=Actin-interacting protein 1;
DE Short=AIP1;
DE AltName: Full=NORI-1;
GN Name=WDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10036186; DOI=10.1006/geno.1998.5672;
RA Adler H.J., Winnicki R.S., Gong T.-W.L., Lomax M.I.;
RT "A gene upregulated in the acoustically damaged chick basilar papilla
RT encodes a novel WD40 repeat protein.";
RL Genomics 56:59-69(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphoid tissue;
RA Abe Y., Nezu K., Ueda N.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-185.
RC TISSUE=Colon, Eye, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-17 (ISOFORMS 1/2).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-606 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PROTEIN SEQUENCE OF 290-306 (ISOFORMS 1/2), AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-81; LYS-95; LYS-115
RP AND LYS-480, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=22721921; DOI=10.1016/j.ejcb.2012.05.005;
RA Cervero P., Himmel M., Kruger M., Linder S.;
RT "Proteomic analysis of podosome fractions from macrophages reveals
RT similarities to spreading initiation centres.";
RL Eur. J. Cell Biol. 91:908-922(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction
CC with ADF/cofilin family proteins (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cell projection, podosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75083-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75083-3; Sequence=VSP_012926;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family.
CC -!- SIMILARITY: Contains 11 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05045.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC -----------------------------------------------------------------------
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DR EMBL; AF020056; AAD05044.1; -; mRNA.
DR EMBL; AF020260; AAD05045.1; ALT_SEQ; mRNA.
DR EMBL; AB010427; BAA31855.2; -; mRNA.
DR EMBL; AK291614; BAF84303.1; -; mRNA.
DR EMBL; AC005674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000201; AAH00201.1; -; mRNA.
DR EMBL; BC002489; AAH02489.1; -; mRNA.
DR EMBL; BC030541; AAH30541.1; -; mRNA.
DR EMBL; AL050108; CAB43276.1; -; mRNA.
DR EMBL; AL110208; CAB53674.2; -; mRNA.
DR PIR; T13152; T13152.
DR RefSeq; NP_005103.2; NM_005112.4.
DR RefSeq; NP_059830.1; NM_017491.3.
DR UniGene; Hs.128548; -.
DR ProteinModelPortal; O75083; -.
DR SMR; O75083; 8-606.
DR IntAct; O75083; 7.
DR STRING; 9606.ENSP00000382881; -.
DR PhosphoSite; O75083; -.
DR OGP; O75083; -.
DR REPRODUCTION-2DPAGE; IPI00746165; -.
DR REPRODUCTION-2DPAGE; O75083; -.
DR UCD-2DPAGE; O75083; -.
DR PaxDb; O75083; -.
DR PRIDE; O75083; -.
DR Ensembl; ENST00000382451; ENSP00000371889; ENSG00000071127.
DR Ensembl; ENST00000382452; ENSP00000371890; ENSG00000071127.
DR Ensembl; ENST00000499869; ENSP00000427687; ENSG00000071127.
DR Ensembl; ENST00000502702; ENSP00000426725; ENSG00000071127.
DR GeneID; 9948; -.
DR KEGG; hsa:9948; -.
DR UCSC; uc021xlv.1; human.
DR CTD; 9948; -.
DR GeneCards; GC04M010075; -.
DR HGNC; HGNC:12754; WDR1.
DR HPA; CAB020804; -.
DR MIM; 604734; gene.
DR neXtProt; NX_O75083; -.
DR PharmGKB; PA37358; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG000780; -.
DR OMA; NYWDSET; -.
DR OrthoDB; EOG7TXKG1; -.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; O75083; -.
DR ChiTaRS; WDR1; human.
DR GeneWiki; WDR1; -.
DR GenomeRNAi; 9948; -.
DR NextBio; 37534; -.
DR PRO; PR:O75083; -.
DR ArrayExpress; O75083; -.
DR Bgee; O75083; -.
DR CleanEx; HS_WDR1; -.
DR Genevestigator; O75083; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 606 WD repeat-containing protein 1.
FT /FTId=PRO_0000051341.
FT REPEAT 56 95 WD 1.
FT REPEAT 100 143 WD 2.
FT REPEAT 144 184 WD 3.
FT REPEAT 187 226 WD 4.
FT REPEAT 232 271 WD 5.
FT REPEAT 318 359 WD 6.
FT REPEAT 363 401 WD 7.
FT REPEAT 443 482 WD 8.
FT REPEAT 487 526 WD 9.
FT REPEAT 530 569 WD 10.
FT REPEAT 574 605 WD 11.
FT MOD_RES 28 28 N6-acetyllysine.
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 95 95 N6-acetyllysine.
FT MOD_RES 115 115 N6-acetyllysine.
FT MOD_RES 238 238 Phosphotyrosine.
FT MOD_RES 480 480 N6-acetyllysine.
FT VAR_SEQ 47 186 Missing (in isoform 2).
FT /FTId=VSP_012926.
FT VARIANT 185 185 I -> V (in dbSNP:rs13441).
FT /FTId=VAR_013445.
SQ SEQUENCE 606 AA; 66194 MW; 8C08C31D5CD097F1 CRC64;
MPYEIKKVFA SLPQVERGVS KIIGGDPKGN NFLYTNGKCV ILRNIDNPAL ADIYTEHAHQ
VVVAKYAPSG FYIASGDVSG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGAV FLWDSGSSVG EITGHNKVIN SVDIKQSRPY RLATGSDDNC AAFFEGPPFK
FKFTIGDHSR FVNCVRFSPD GNRFATASAD GQIYIYDGKT GEKVCALGGS KAHDGGIYAI
SWSPDSTHLL SASGDKTSKI WDVSVNSVVS TFPMGSTVLD QQLGCLWQKD HLLSVSLSGY
INYLDRNNPS KPLHVIKGHS KSIQCLTVHK NGGKSYIYSG SHDGHINYWD SETGENDSFA
GKGHTNQVSR MTVDESGQLI SCSMDDTVRY TSLMLRDYSG QGVVKLDVQP KCVAVGPGGY
AVVVCIGQIV LLKDQRKCFS IDNPGYEPEV VAVHPGGDTV AIGGVDGNVR LYSILGTTLK
DEGKLLEAKG PVTDVAYSHD GAFLAVCDAS KVVTVFSVAD GYSENNVFYG HHAKIVCLAW
SPDNEHFASG GMDMMVYVWT LSDPETRVKI QDAHRLHHVS SLAWLDEHTL VTTSHDASVK
EWTITY
//
MIM
604734
*RECORD*
*FIELD* NO
604734
*FIELD* TI
*604734 WD REPEAT-CONTAINING PROTEIN 1; WDR1
;;ACTIN-INTERACTING PROTEIN 1; AIP1
*FIELD* TX
read more
CLONING
WD repeats are approximately 30- to 40-amino acid domains containing
several conserved residues, including a trp-asp at the C-terminal end.
These domains are involved in protein-protein interactions. WD repeats
have been found in heterotrimeric G proteins and regulatory proteins,
such as those involved in cell division, cell-fate determination, gene
transcription, mRNA modification, transmembrane signaling, and vesicle
fusion. WD repeats typically occur multiple times within a protein. To
identify processes that may play a role in avian inner ear repair, Adler
et al. (1999) used differential display of mRNA to isolate genes that
are upregulated in the avian basilar papilla after acoustic
overstimulation. They identified a chicken gene encoding a protein
composed almost entirely of 9 WD repeats; thus, they named the protein
'WD repeat protein-1' (Wdr1). By searching an EST database using the
sequence of a chicken Wdr1 cDNA as the query, Adler et al. (1999)
identified human and mouse orthologs of WDR1. Like chicken Wdr1, the
predicted human and mouse WDR1 proteins contain 9 WD repeats. The
deduced 606-amino acid human WDR1 protein shares 95% amino acid sequence
identity with mouse Wdr1 and 86% identity with chicken Wdr1. Chicken
Wdr1 has high sequence identity to S. cerevisiae and P. polycephalum WD
repeat-containing proteins that bind actin, suggesting that WDR1
proteins may interact with actin. Adler et al. (1999) deposited the
sequence of a human WDR1 splicing variant that encodes a protein lacking
72 C-terminal amino acids into GenBank (GENBANK AF020260).
MAPPING
By radiation hybrid mapping, Adler et al. (1999) mapped the WDR1 gene to
chromosome 4p. They noted that an EST cluster composed of sequences
identical to the WDR1 gene had been mapped between 22 and 24 cM from the
telomere of chromosome 4p.
ANIMAL MODEL
By generating an allelic series for mouse Wdr1, Kile et al. (2007) found
that reductions in Wdr1 function produced a phenotype gradient. Severe
loss of function caused embryonic lethality, whereas hypomorphic alleles
caused macrothrombocytopenia due to defective megakaryocyte maturation
and autoinflammatory disease due to massive neutrophil infiltration in
lesions. Fluorescence and electron microscopy showed that Wdr1 was
essential for normal motility and actin depolymerization kinetics,
probably through interaction with cofilin (CFL1; 601442). Kile et al.
(2007) concluded that WDR1 is required for megakaryocytes and
neutrophils and that cofilin-mediated actin dynamics are important to
development and function of both cell types.
*FIELD* RF
1. Adler, H. J.; Winnicki, R. S.; Gong, T.-W. L.; Lomax, M. I.: A
gene upregulated in the acoustically damaged chick basilar papilla
encodes a novel WD40 repeat protein. Genomics 56: 59-69, 1999.
2. Kile, B. T.; Panopoulos, A. D.; Stirzaker, R. A.; Hacking, D. F.;
Tahtamouni, L. H.; Willson, T. A.; Mielke, L. A.; Henley, K. J.; Zhang,
J.-G.; Wicks, I. P.; Stevenson, W. S.; Nurden, P.; Watowich, S. S.;
Justice, M. J.: Mutations in the cofilin partner Aip1/Wdr1 cause
autoinflammatory disease and macrothrombocytopenia. Blood 110: 2371-2380,
2007.
*FIELD* CN
Paul J. Converse - updated: 7/24/2008
*FIELD* CD
Patti M. Sherman: 3/23/2000
*FIELD* ED
mgross: 08/18/2008
terry: 7/24/2008
mcapotos: 4/7/2000
psherman: 3/24/2000
*RECORD*
*FIELD* NO
604734
*FIELD* TI
*604734 WD REPEAT-CONTAINING PROTEIN 1; WDR1
;;ACTIN-INTERACTING PROTEIN 1; AIP1
*FIELD* TX
read more
CLONING
WD repeats are approximately 30- to 40-amino acid domains containing
several conserved residues, including a trp-asp at the C-terminal end.
These domains are involved in protein-protein interactions. WD repeats
have been found in heterotrimeric G proteins and regulatory proteins,
such as those involved in cell division, cell-fate determination, gene
transcription, mRNA modification, transmembrane signaling, and vesicle
fusion. WD repeats typically occur multiple times within a protein. To
identify processes that may play a role in avian inner ear repair, Adler
et al. (1999) used differential display of mRNA to isolate genes that
are upregulated in the avian basilar papilla after acoustic
overstimulation. They identified a chicken gene encoding a protein
composed almost entirely of 9 WD repeats; thus, they named the protein
'WD repeat protein-1' (Wdr1). By searching an EST database using the
sequence of a chicken Wdr1 cDNA as the query, Adler et al. (1999)
identified human and mouse orthologs of WDR1. Like chicken Wdr1, the
predicted human and mouse WDR1 proteins contain 9 WD repeats. The
deduced 606-amino acid human WDR1 protein shares 95% amino acid sequence
identity with mouse Wdr1 and 86% identity with chicken Wdr1. Chicken
Wdr1 has high sequence identity to S. cerevisiae and P. polycephalum WD
repeat-containing proteins that bind actin, suggesting that WDR1
proteins may interact with actin. Adler et al. (1999) deposited the
sequence of a human WDR1 splicing variant that encodes a protein lacking
72 C-terminal amino acids into GenBank (GENBANK AF020260).
MAPPING
By radiation hybrid mapping, Adler et al. (1999) mapped the WDR1 gene to
chromosome 4p. They noted that an EST cluster composed of sequences
identical to the WDR1 gene had been mapped between 22 and 24 cM from the
telomere of chromosome 4p.
ANIMAL MODEL
By generating an allelic series for mouse Wdr1, Kile et al. (2007) found
that reductions in Wdr1 function produced a phenotype gradient. Severe
loss of function caused embryonic lethality, whereas hypomorphic alleles
caused macrothrombocytopenia due to defective megakaryocyte maturation
and autoinflammatory disease due to massive neutrophil infiltration in
lesions. Fluorescence and electron microscopy showed that Wdr1 was
essential for normal motility and actin depolymerization kinetics,
probably through interaction with cofilin (CFL1; 601442). Kile et al.
(2007) concluded that WDR1 is required for megakaryocytes and
neutrophils and that cofilin-mediated actin dynamics are important to
development and function of both cell types.
*FIELD* RF
1. Adler, H. J.; Winnicki, R. S.; Gong, T.-W. L.; Lomax, M. I.: A
gene upregulated in the acoustically damaged chick basilar papilla
encodes a novel WD40 repeat protein. Genomics 56: 59-69, 1999.
2. Kile, B. T.; Panopoulos, A. D.; Stirzaker, R. A.; Hacking, D. F.;
Tahtamouni, L. H.; Willson, T. A.; Mielke, L. A.; Henley, K. J.; Zhang,
J.-G.; Wicks, I. P.; Stevenson, W. S.; Nurden, P.; Watowich, S. S.;
Justice, M. J.: Mutations in the cofilin partner Aip1/Wdr1 cause
autoinflammatory disease and macrothrombocytopenia. Blood 110: 2371-2380,
2007.
*FIELD* CN
Paul J. Converse - updated: 7/24/2008
*FIELD* CD
Patti M. Sherman: 3/23/2000
*FIELD* ED
mgross: 08/18/2008
terry: 7/24/2008
mcapotos: 4/7/2000
psherman: 3/24/2000